EC 1.14.13.17      
Transferred entry: cholesterol 7α-monooxygenase. Now EC 1.14.14.23, cholesterol 7α-monooxygenase
[EC 1.14.13.17 created 1976, deleted 2016]
 
 
EC 1.14.13.170     
Accepted name: pentalenolactone D synthase
Reaction: 1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = pentalenolactone D + NADP+ + H2O
Glossary: 1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
pentalenolactone D = (1S,4aR,6aS,9aR)-1,8,8-trimethyl-2-oxo-1,2,4,4a,6a,7,8,9-octahydropentaleno[1,6a-c]pyran-5-carboxylate
Other name(s): penE (gene name); pntE (gene name)
Systematic name: 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (pentalenolactone-D forming)
Comments: A FAD-dependent oxygenase. Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae. The ketone undergoes a biological Baeyer-Villiger reaction. Part of the pathway of pentalenolactone biosynthesis.
References:
1.  Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739–1754. [PMID: 21250661]
[EC 1.14.13.170 created 2012]
 
 
EC 1.14.13.171     
Accepted name: neopentalenolactone D synthase
Reaction: 1-deoxy-11-oxopentalenate + NADPH + H+ + O2 = neopentalenolactone D + NADP+ + H2O
Glossary: 1-deoxy-11-oxopentalenate = (1S,3aR,5aS)-1,7,7-trimethyl-2-oxo-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylate
neopentalenolactone D = (1S,4aR,6aS)-1,7,7-trimethyl-3-oxo-4,4a,6a,7,8,9-hexahydro-3H-pentaleno[6a,1-c]pyran-5-carboxylate
Other name(s): ptlE (gene name)
Systematic name: 1-deoxy-11-oxopentalenate,NADH:oxygen oxidoreductase (neopentalenolactone-D forming)
Comments: A FAD-dependent oxygenase. Isolated from the bacterium Streptomyces avermitilis. The ketone undergoes a biological Baeyer-Villiger reaction.
References:
1.  Seo, M.J., Zhu, D., Endo, S., Ikeda, H. and Cane, D.E. Genome mining in Streptomyces. Elucidation of the role of Baeyer-Villiger monooxygenases and non-heme iron-dependent dehydrogenase/oxygenases in the final steps of the biosynthesis of pentalenolactone and neopentalenolactone. Biochemistry 50 (2011) 1739–1754. [PMID: 21250661]
[EC 1.14.13.171 created 2012]
 
 
EC 1.14.13.172     
Accepted name: salicylate 5-hydroxylase
Reaction: salicylate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
Glossary: 2,5-dihydroxybenzoate = gentisate
Other name(s): nagG (gene name); nagH (gene name)
Systematic name: salicylate,NADH:oxygen oxidoreductase (5-hydroxylating)
Comments: This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin—NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
References:
1.  Fuenmayor, S.L., Wild, M., Boyes, A.L. and Williams, P.A. A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J. Bacteriol. 180 (1998) 2522–2530. [PMID: 9573207]
[EC 1.14.13.172 created 2013]
 
 
EC 1.14.13.173      
Transferred entry: 11-oxo-β-amyrin 30-oxidase. Now EC 1.14.14.115, 11-oxo-β-amyrin 30-oxidase.
[EC 1.14.13.173 created 2013, deleted 2018]
 
 
EC 1.14.13.174      
Transferred entry: averantin hydroxylase. Now EC 1.14.14.116, averantin hydroxylase
[EC 1.14.13.174 created 2013, deleted 2018]
 
 
EC 1.14.13.175      
Transferred entry: aflatoxin B synthase. Now EC 1.14.14.117, aflatoxin B synthase
[EC 1.14.13.175 created 2013, deleted 2018]
 
 
EC 1.14.13.176      
Transferred entry: tryprostatin B 6-hydroxylase. Now EC 1.14.14.118, tryprostatin B 6-hydroxylase
[EC 1.14.13.176 created 2013, deleted 2018]
 
 
EC 1.14.13.177      
Transferred entry: fumitremorgin C monooxygenase. Now EC 1.14.14.119, fumitremorgin C monooxygenase
[EC 1.14.13.177 created 2013, deleted 2018]
 
 
EC 1.14.13.178     
Accepted name: methylxanthine N1-demethylase
Reaction: (1) caffeine + O2 + NAD(P)H + H+ = theobromine + NAD(P)+ + H2O + formaldehyde
(2) theophylline + O2 + NAD(P)H + H+ = 3-methylxanthine + NAD(P)+ + H2O + formaldehyde
(3) paraxanthine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
Glossary: caffeine = 1,3,7-trimethylxanthine
theobromine = 3,7-dimethylxanthine
theophylline = 1,3-dimethylxanthine
paraxanthine = 1,7-dimethylxanthine
Other name(s): ndmA (gene name)
Systematic name: caffeine:oxygen oxidoreductase (N1-demethylating)
Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, methylxanthine N3-demethylase, and has a 5-fold higher activity with NADH than with NADPH [2]. Also demethylate 1-methylxantine with lower efficiency. Forms part of the degradation pathway of methylxanthines.
References:
1.  Summers, R.M., Louie, T.M., Yu, C.L. and Subramanian, M. Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. Microbiology 157 (2011) 583–592. [PMID: 20966097]
2.  Summers, R.M., Louie, T.M., Yu, C.L., Gakhar, L., Louie, K.C. and Subramanian, M. Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. J. Bacteriol. 194 (2012) 2041–2049. [PMID: 22328667]
[EC 1.14.13.178 created 2013]
 
 
EC 1.14.13.179     
Accepted name: methylxanthine N3-demethylase
Reaction: (1) theobromine + O2 + NAD(P)H + H+ = 7-methylxanthine + NAD(P)+ + H2O + formaldehyde
(2) 3-methylxanthine + O2 + NAD(P)H + H+ = xanthine + NAD(P)+ + H2O + formaldehyde
Glossary: theobromine = 3,7-dimethylxanthine
Other name(s): ndmB (gene name)
Systematic name: theobromine:oxygen oxidoreductase (N3-demethylating)
Comments: A non-heme iron oxygenase. The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, methylxanthine N1-demethylase, and has higher activity with NADH than with NADPH [1]. Also demethylates caffeine and theophylline with lower efficiency. Forms part of the degradation pathway of methylxanthines.
References:
1.  Summers, R.M., Louie, T.M., Yu, C.L. and Subramanian, M. Characterization of a broad-specificity non-haem iron N-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. Microbiology 157 (2011) 583–592. [PMID: 20966097]
2.  Summers, R.M., Louie, T.M., Yu, C.L., Gakhar, L., Louie, K.C. and Subramanian, M. Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. J. Bacteriol. 194 (2012) 2041–2049. [PMID: 22328667]
[EC 1.14.13.179 created 2013]
 
 


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